Evidence map›Paper›PMID 26249356›Full record

ArticleActa crystallographica. Section D, Biological crystallography2015

Fully automatic characterization and data collection from crystals of biological macromolecules.

Olof Svensson, Stéphanie Malbet-Monaco, Alexander Popov, Didier Nurizzo, Matthew W Bowler

Abstract read
In one paragraph

Article in Acta crystallographica. Section D, Biological crystallography, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 70 papers.

0numbers the graph read from it
0cells of the map it votes in
70citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

70 citing papers in PubMed.

  1. Article
  2. Automated workflows for strategy computation and data collection at synchrotron beamlines.Acta crystallographica. Section D, Structural biology · 2026
    Article
  3. Article
  4. Article
  5. Article
  6. Enhanced capabilities for multi-crystal data collection based on double mesh scans.Acta crystallographica. Section D, Structural biology · 2025
    Article
  7. Article
  8. Review
  9. Article
  10. Article
  11. Structural Biology for Target Identification and Validation.Methods in molecular biology (Clifton, N.J.) · 2025
    Article
  12. Article
  13. Identifying and avoiding radiation damage in macromolecular crystallography.Acta crystallographica. Section D, Structural biology · 2024
    Article
  14. Article
  15. Structural basis of centromeric cohesion protection.Nature structural & molecular biology · 2023
    Article
  16. Article
  17. Crystal structure of MAB_4123, a putative flavin-dependent monooxygenase from Mycobacterium abscessus.Acta crystallographica. Section F, Structural biology communications · 2023
    Article
  18. Article
  19. Article
  20. Article

10 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

5 authors.

Olof SvenssonEuropean Synchrotron Radiation Facility, 71 Avenue des Martyrs, CS 40220, 38043 Grenoble, France.
Stéphanie Malbet-MonacoEuropean Synchrotron Radiation Facility, 71 Avenue des Martyrs, CS 40220, 38043 Grenoble, France.
Alexander PopovEuropean Synchrotron Radiation Facility, 71 Avenue des Martyrs, CS 40220, 38043 Grenoble, France.
Didier NurizzoEuropean Synchrotron Radiation Facility, 71 Avenue des Martyrs, CS 40220, 38043 Grenoble, France.
Matthew W BowlerEuropean Molecular Biology Laboratory, Grenoble Outstation, 71 Avenue des Martyrs, CS 90181, 38042 Grenoble, France.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Considerable effort is dedicated to evaluating macromolecular crystals at synchrotron sources, even for well established and robust systems. Much of this work is repetitive, and the time spent could be better invested in the interpretation of the results. In order to decrease the need for manual intervention in the most repetitive steps of structural biology projects, initial screening and data collection, a fully automatic system has been developed to mount, locate, centre to the optimal diffraction volume, characterize and, if possible, collect data from multiple cryocooled crystals. Using the capabilities of pixel-array detectors, the system is as fast as a human operator, taking an average of 6 min per sample depending on the sample size and the level of characterization required. Using a fast X-ray-based routine, samples are located and centred systematically at the position of highest diffraction signal and important parameters for sample characterization, such as flux, beam size and crystal volume, are automatically taken into account, ensuring the calculation of optimal data-collection strategies. The system is now in operation at the new ESRF beamline MASSIF-1 and has been used by both industrial and academic users for many different sample types, including crystals of less than 20 µm in the smallest dimension. To date, over 8000 samples have been evaluated on MASSIF-1 without any human intervention.

Indexed as

AlgorithmsCrystallography, X-RayImage Processing, Computer-AssistedMacromolecular SubstancesMacromolecular Substancesautomationmacromolecular crystallographysynchrotron instrumentationX-ray crystal centring

Identifiers

PMID26249356
PMCPMC4528805

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Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.